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P94248 (BGLFU_BIFBR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional beta-D-glucosidase/beta-D-fucosidase

EC=3.2.1.21
EC=3.2.1.38
OrganismBifidobacterium breve
Taxonomic identifier1685 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional beta-D-glucosidase/beta-D-fucosidase. Activity towards pNP-beta-D-fucoside is about 80-85% of the activity towards pNP-beta-D-glucoside. Also has slight activity (less than 10%) towards pNP-beta-D-galactoside, and very low activity (less than 1%) towards pNP-beta-D-xyloside. Hydrolyzes laminaribiose, sophorose, cellobiose and gentobiose. Not active against maltose, pNP-alpha-D-glucoside or pNP-beta-L-fucoside. Ref.1 Ref.2

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Ref.1 Ref.2

Hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides. Ref.1 Ref.2

Enzyme regulation

Inhibited by Cu2+, Ag+ and Hg+, but not by other cations such as Mg2+, Ca2+, Mn2+ and Co2+. Inhibited by 1-amino-1-deoxy-D-glucose and p-chloromercuribenzoic acid, but not by EDTA or dithiothreitol. Inhibited by the disaccharides sucrose, lactose and cellobiose. The monosaccharides D-fructose, D-mannose, D-xylose and D-glucose increase the beta-D-fucosidase activity, but not the beta-D-glucosidase activity. D-glucose inhibits the beta-D-glucosidase activity, but promotes the beta-D-fucosidase activity. D-fucose inhibits the beta-D-glucosidase activity and does not significantly affect the beta-D-fucosidase activity. Ref.2

Subunit structure

Monomer. Ref.2

Subcellular location

Secreted Ref.2.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.3 mM for pNP-beta-D-glucoside Ref.1 Ref.2

KM=0.7 mM for pNP-beta-D-fucoside Ref.2

pH dependence:

Optimum pH is 5.5 with pNP-beta-D-glucoside as a substrate. Retains more than 90% of its activity between pH 5.0 and 7.0. Retains 70% of its activity at pH 4.5 and 8.5. Ref.1 Ref.2

Temperature dependence:

Optimum temperature is 45 degrees Celsius with pNP-beta-D-glucoside as a substrate. Retains 60% of its activity after 10 minutes incubation at 50 degrees Celsius. Ref.1 Ref.2

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-D-fucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

beta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 460459Bifunctional beta-D-glucosidase/beta-D-fucosidase Ref.2
PRO_0000395428

Sites

Active site1681Proton donor By similarity UniProtKB Q25BW5
Active site3621Nucleophile By similarity UniProtKB Q25BW5

Sequences

Sequence LengthMass (Da)Tools
P94248 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 5FD80CB8AB6888A9

FASTA46051,514
        10         20         30         40         50         60 
MTMIFPKGFM FGTATAAYQI EGAVAEGGRT PSIWDTFSHT GHTLNGDTGD VADDFYHRWE 

        70         80         90        100        110        120 
DDLKLLRDLG VNAYRFSIGI PRVIPTPDGK PNQEGLDFYS RIVDRLLEYG IAPIVTLYHW 

       130        140        150        160        170        180 
DLPQYMASGD GREGGWLERE TAYRIADYAG IVAKCLGDRV HTYTTLNEPW CSAHLSYGGT 

       190        200        210        220        230        240 
EHAPGLGAGP LAFRAAHHLN LAHGLMCEAV RAEAGAKPGL SVTLNLQICR GDADAVHRVD 

       250        260        270        280        290        300 
LIGNRVFLDP MLRGRYPDEL FSITKGICDW GFVCDGDLDL IHQPIDVLGL NYYSTNLVKM 

       310        320        330        340        350        360 
SDRPQFPQST EASTAPGASD VDWLPTAGPH TEMGWNIDPD ALYETLVRLN DNYPGMPLVV 

       370        380        390        400        410        420 
TENGMACPDK VEVGTDGVKM VHDNDRIDYL RRHLEAVYRA IEEGTDVRGY FAWSLMDNFE 

       430        440        450        460 
WAFGYSKRFG LTYVDYESQE RVKKDSFDWY RRFIADHSAR 

« Hide

References

[1]"Cloning and nucleotide sequence of the beta-D-glucosidase gene from Bifidobacterium breve clb, and expression of beta-D-glucosidase activity in Escherichia coli."
Nunoura N., Ohdan K., Tanaka K., Tamaki H., Yano T., Inui M., Yukawa H., Yamamoto K., Kumagai H.
Biosci. Biotechnol. Biochem. 60:2011-2018(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"Purification and characterization of beta-D-glucosidase (beta-D-fucosidase) from Bifidobacterium breve clb acclimated to cellobiose."
Nunoura N., Ohdan K., Yano T., Yamamoto K., Kumagai H.
Biosci. Biotechnol. Biochem. 60:188-193(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-30, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88311 Genomic DNA. Translation: BAA19881.1.
PIRJC5137.

3D structure databases

ProteinModelPortalP94248.
SMRP94248. Positions 2-458.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR03356. BGL. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLFU_BIFBR
AccessionPrimary (citable) accession number: P94248
Secondary accession number(s): O08487
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: May 1, 1997
Last modified: October 16, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries